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Competition for shared downstream signaling molecules establishes indirect negative feedback between EGFR and EphA2.
Oh, Dongmyung; Chen, Zhongwen; Biswas, Kabir H; Bai, Funing; Ong, Hui Ting; Sheetz, Michael P; Groves, Jay T.
Afiliação
  • Oh D; Mechanobiology Institute, National University of Singapore, Singapore, Singapore; Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, Texas.
  • Chen Z; Mechanobiology Institute, National University of Singapore, Singapore, Singapore; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Science, Shanghai, China.
  • Biswas KH; Mechanobiology Institute, National University of Singapore, Singapore, Singapore; Division of Biological and Biomedical Sciences, College of Health & Life Sciences, Hamad Bin Khalifa University, Qatar Foundation, Doha, Qatar.
  • Bai F; Mechanobiology Institute, National University of Singapore, Singapore, Singapore.
  • Ong HT; Mechanobiology Institute, National University of Singapore, Singapore, Singapore.
  • Sheetz MP; Mechanobiology Institute, National University of Singapore, Singapore, Singapore; Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, Texas. Electronic address: misheetz@utmb.edu.
  • Groves JT; Department of Chemistry, University of California, Berkeley, California; Institute for Digital Molecular Analytics and Science, Nanyang Technological University, Singapore, Singapore. Electronic address: jtgroves@lbl.gov.
Biophys J ; 121(10): 1897-1908, 2022 05 17.
Article em En | MEDLINE | ID: mdl-35430415
Cells sense a variety of extracellular growth factors and signaling molecules through numerous distinct receptor tyrosine kinases (RTKs) on the cell surface. In many cases, the same intracellular signaling molecules interact with more than one type of RTK. How signals from different RTKs retain the identity of the triggering receptor and how (or if) different receptors may synergize or compete remain largely unknown. Here we utilize an experimental strategy, combining microscale patterning and single-molecule imaging, to measure the competition between ephrin-A1:EphA2 and epidermal growth factor (EGF):EGF receptor (EGFR) ligand-receptor complexes for the shared downstream signaling molecules, Grb2 and SOS. The results reveal a distinct hierarchy, in which newly formed EGF:EGFR complexes outcompete ephrin-A1:EphA2 for Grb2 and SOS, revealing a type of negative crosstalk interaction fundamentally controlled by chemical mass action and protein copy number limitations.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Receptor EphA2 / Efrina-A1 Idioma: En Revista: Biophys J Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Receptor EphA2 / Efrina-A1 Idioma: En Revista: Biophys J Ano de publicação: 2022 Tipo de documento: Article